Cited by 266PI3K/AKT/mTOR signaling in cancerAutophagy in Disease and TherapyMetabolism, Diabetes, and Cancer

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Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9

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Jung, Jennifer, Genau, Heide Marika, Behrends, Christian·2015·Molecular and Cellular Biology

DOI 10.1128/mcb.00125-15PMC PMC4475919

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Abstract

The serine/threonine kinase mTORC1 regulates cellular homeostasis in response to many cues, such as nutrient status and energy level. Amino acids induce mTORC1 activation on lysosomes via the small Rag GTPases and the Ragulator complex, thereby controlling protein translation and cell growth. Here, we identify the human 11-pass transmembrane protein SLC38A9 as a novel component of the Rag-Ragulator complex. SLC38A9 localizes with Rag-Ragulator complex components on lysosomes and associates with Rag GTPases in an amino acid-sensitive and nucleotide binding state-dependent manner. Depletion of SLC38A9 inhibits mTORC1 activity in the presence of amino acids and in response to amino acid replenishment following starvation. Conversely, SLC38A9 overexpression causes RHEB (Ras homolog enriched in brain) GTPase-dependent hyperactivation of mTORC1 and partly sustains mTORC1 activity upon amino acid deprivation. Intriguingly, during amino acid starvation mTOR is retained at the lysosome upon SLC38A9 depletion but fails to be activated. Together, the findings of our study reveal SLC38A9 as a Rag-Ragulator complex member transducing amino acid availability to mTORC1 activity.

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Predicting transmembrane protein topology with a hidden markov model: application to complete genomes11Edited by F. Cohen
Krogh, A., Larsson, B., von Heijne, G., & Sonnhammer, E. L. L. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4315 · Cited by 12,654
Antimicrobial Autophagy: A Conserved Innate Immune Response in Drosophila
Moy, R. H., & Cherry, S. R. (2013) · Journal of Innate Immunity · doi:10.1159/000350326 · Cited by 3,551
mTOR Interacts with Raptor to Form a Nutrient-Sensitive Complex that Signals to the Cell Growth Machinery
Kim, D., Sarbassov, D. D., Ali, S. M., King, J. E., Latek, R. R., Erdjument‐Bromage, H., Tempst, P., & Sabatini, D. M. (2002) · Cell · doi:10.1016/s0092-8674(02)00808-5 · Cited by 3,051
Defining the role of mTOR in cancer
Guertin, D. A., & Sabatini, D. M. (2007) · Cancer Cell · doi:10.1016/j.ccr.2007.05.008 · Cited by 2,833
The Rag GTPases Bind Raptor and Mediate Amino Acid Signaling to mTORC1
Sancak, Y., Peterson, T. R., Shaul, Y. D., Lindquist, R. A., Thoreen, C. C., Bar-Peled, L., & Sabatini, D. M. (2008) · Science · doi:10.1126/science.1157535 · Cited by 2,773
Ragulator-Rag Complex Targets mTORC1 to the Lysosomal Surface and Is Necessary for Its Activation by Amino Acids
Sancak, Y., Bar-Peled, L., Zoncu, R., Markhard, A. L., Nada, S., & Sabatini, D. M. (2010) · Cell · doi:10.1016/j.cell.2010.02.024 · Cited by 2,464 · cited 13×
“Cycling of mTOR between cytosol and lysosome generally is coupled to its inactive and active states, respectively, and depends on Rag GTPases, Ragulator, TSC, and RHEB GTPase (9, 16, 23, 31).”
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Rheb GTPase is a direct target of TSC2 GAP activity and regulates mTOR signaling
Inoki, K., Li, Y., Xu, T., & Guan, K.-L. (2003) · Genes & Development · doi:10.1101/gad.1110003 · Cited by 1,911
Bidirectional Transport of Amino Acids Regulates mTOR and Autophagy
Nicklin, P., Bergman, P., Zhang, B., Triantafellow, E., Wang, H., Nyfeler, B., Yang, H., Hild, M., Kung, C., Wilson, C., et al. (2009) · Cell · doi:10.1016/j.cell.2008.11.044 · Cited by 1,798
A tissue-specific atlas of mouse protein phosphorylation and expression
Huttlin, E. L., Jedrychowski, M. P., Elias, J. E., Goswami, T., Rad, R., Beausoleil, S. A., Villén, J., Haas, W., Sowa, M. E., & Gygi, S. P. (2010) · Cell · doi:10.1016/j.cell.2010.12.001 · Cited by 1,778
Drug—target network
Yıldırım, M. A., Goh, K.-I., Cusick, M. E., Barabási, A.-Ĺ., & Vidal, M. (2007) · Nature Biotechnology · doi:10.1038/nbt1338 · Cited by 1,744
mTORC1 Senses Lysosomal Amino Acids Through an Inside-Out Mechanism That Requires the Vacuolar H + -ATPase
Zoncu, R., Bar-Peled, L., Efeyan, A., Wang, S., Sancak, Y., & Sabatini, D. M. (2011) · Science · doi:10.1126/science.1207056 · Cited by 1,673
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Sowa, M. E., Bennett, E. J., Gygi, S. P., & Harper, J. W. (2009) · Cell · doi:10.1016/j.cell.2009.04.042 · Cited by 1,523
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Hara, K., Yonezawa, K., Weng, Q.-P., Kozlowski, M. T., BELHAM, C. M., & Avruch, J. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.23.14484 · Cited by 1,370
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Sengupta, S., Peterson, T. R., & Sabatini, D. M. (2010) · Molecular Cell · doi:10.1016/j.molcel.2010.09.026 · Cited by 1,275
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Bar-Peled, L., Chantranupong, L., Cherniack, A. D., Chen, W. W., Ottina, K. A., Grabiner, B. C., Spear, E. D., Carter, S. L., Meyerson, M., & Sabatini, D. M. (2013) · Science · doi:10.1126/science.1232044 · Cited by 1,080 · cited 4×
“While the GATOR1 (GAP activity toward Rags) complex exhibits GAP activity toward RagA/B (21), FLCN (folliculin) and its interacting partners, FNIP1 (folliculin-interacting protein 1) and FNIP2, act on RagC/D (20).”
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Tee, A. R., Manning, B. D., Roux, P. P., Cantley, L. C., & Blenis, J. (2003) · Current Biology · doi:10.1016/s0960-9822(03)00506-2 · Cited by 1,080
Rheb Binds and Regulates the mTOR Kinase
Long, X., Lin, Y., Ortiz-Vega, S., Yonezawa, K., & Avruch, J. (2005) · Current Biology · doi:10.1016/j.cub.2005.02.053 · Cited by 1,005
GβL, a Positive Regulator of the Rapamycin-Sensitive Pathway Required for the Nutrient-Sensitive Interaction between Raptor and mTOR
Kim, D., Sarbassov, D. D., Ali, S. M., Latek, R. R., Guntur, K., Erdjument‐Bromage, H., Tempst, P., & Sabatini, D. M. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00114-x · Cited by 992
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“Cycling of mTOR between cytosol and lysosome generally is coupled to its inactive and active states, respectively, and depends on Rag GTPases, Ragulator, TSC, and RHEB GTPase (9, 16, 23, 31).”
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Lysosomal amino acid transporter SLC38A9 signals arginine sufficiency to mTORC1
Wang, S., Tsun, Z.-Y., Wolfson, R. L., Shen, K., Wyant, G. A., Plovanich, M., Yuan, E. D., Jones, T. D., Chantranupong, L., Comb, W. C., et al. (2015) · Science · doi:10.1126/science.1257132 · Cited by 865
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Changes in lysosome shape and distribution correlated with changes in cytoplasmic pH
Heuser, J. (1989) · The Journal of cell biology · doi:10.1083/jcb.108.3.855 · Cited by 390
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Smith, E. M., FINN, S. G., Tee, A. R., Browne, G. J., & Proud, C. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414499200 · Cited by 354
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Evidence for the transport of neutral as well as cationic amino acids by ATA3, a novel and liver-specific subtype of amino acid transport system A
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Hundal, H. S. (2011) · Frontiers in Bioscience-Elite · doi:10.2741/e332 · Cited by 97
Rheb and Rags come together at the lysosome to activate mTORC1
Groenewoud, M. J., & Zwartkruis, F. J. T. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130037 · Cited by 96
mTOR direct interactions with Rheb-GTPase and raptor: sub-cellular localization using fluorescence lifetime imaging
Yadav, R. B., Burgos, P., Parker, A. W., Iadevaia, V., Proud, C. G., Allen, R. A., O’Connell, J. P., Jeshtadi, A., Stubbs, C. D., & Botchway, S. W. (2013) · BMC Cell Biology · doi:10.1186/1471-2121-14-3 · Cited by 71
Lysosomal amino acid transporter LYAAT‐1 in the rat central nervous system: An in situ hybridization and immunohistochemical study
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Amino acid derivatives are substrates or non-transported inhibitors of the amino acid transporter PAT2 (slc36a2)
Edwards, N., Anderson, C. M. H., Gatfield, K. M., Jevons, M., Ganapathy, V., & Thwaites, D. T. (2010) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2010.07.032 · Cited by 30
Influence of Cycloheximide on the Synthesis and Utilization of Amino Acids in Suspension Cultures
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Widuczynski, I., & Stoppani, A. O. M. (1965) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/0304-4165(65)90347-8 · Cited by 21
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Authors: Jung, J., Genau, H. M., & Behrends, C.
Affiliations: Goethe University Frankfurt (DE)
Corresponding author: Behrends, Christian
ORCID: Jung, Jennifer
Behrends, Christian
Venue: Molecular and Cellular Biology
Publisher: Informa UK Limited
Published: 2015-07-01
Volume: 35
Issue: 14
Pages: 2479-2494
ISSN: 0270-7306 (ISSN-L)
1098-5549
DOI: 10.1128/mcb.00125-15
PMC: PMC4475919
OpenAlex: W2257572427
Cited by: 266
References: 55
Citations by year: 2026: 9 · 2025: 11 · 2024: 16 · 2023: 23 · 2022: 23 · 2021: 37 · 2020: 20 · 2019: 28 · 2018: 29 · 2017: 33 · 2016: 30 · 2015: 6
FWCI: 14.19
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: journals.asm.org/non-commercial-tdm-license (tdm)
Locations: Molecular and Cellular Biology (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
Funders: Deutsche Forschungsgemeinschaft (BE 4685/1‐1)
FP7 Ideas: European Research Council (282333)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Metabolism, Diabetes, and Cancer
Keywords: SLC38A9, mTORC1, Rag GTPases, amino acid signaling, lysosomes, Rheb, amino acid starvation, transmembrane proteins, translational regulation
MeSH terms: Ras Homolog Enriched in Brain Protein, Mechanistic Target of Rapamycin Complex 1, Amino Acids, Fluorescent Antibody Technique, Humans, Lysosomes, Neuropeptides, Protein Binding, Immunoblotting, GTP Phosphohydrolases, Monomeric GTP-Binding Proteins, Amino Acid Transport Systems, RNA Interference, Multiprotein Complexes, HEK293 Cells, TOR Serine-Threonine Kinases, Protein Interaction Maps

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Amino Acid-Dependent mTORC1 Regulation by the Lysosomal Membrane Protein SLC38A9

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